Journal
TOXICON
Volume 107, Issue -, Pages 187-196Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.toxicon.2015.07.008
Keywords
Aipysurus laevis; Olive sea snake; Snake venom; Proteomics; Toxicity; Venomics
Categories
Funding
- Drug Research Academy (University of Copenhagen)
- Novo Nordisk Fonden [NNF130C0005613]
- Dansk Tennis Fond Oticon Fonden [14-0857]
- Knud Hojgaards Fond
- Rudolph Als Fondet
- Henry Shaws Legat
- Laege Johannes Nicolai Krigsgaard of Hustru Else Krogsgaards Mindelegat for Medicinsk Forskning og Medicinske Studenter ved Kobenhavns Universitet
- Lundbeckfonden [R169-2014-833]
- Torben of Alice Frimodts Fond
- Frants Allings Legat
- Christian og Ottilia Brorsons Rejselegat for Yngre Videnskabsmndog-kvinder
- Fonden for Laegevidenskabens Fremme [14-253]
- Novo Nordisk Fonden [NNF13OC0005613] Funding Source: researchfish
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Four specimens of the olive sea snake, Aipysurus laevis, were collected off the coast of Western Australia, and the venom proteome was characterized and quantitatively estimated by RP-HPLC, SDS-PAGE, and MALDI-TOF-TOF analyses. A. laevis venom is remarkably simple and consists of phospholipases A(2) (71.2%), three-finger toxins (3FTx; 25.3%), cysteine-rich secretory proteins (CRISP; 2.5%), and traces of a complement control module protein (CCM; 0.2%). Using a Toxicity Score, the most lethal components were determined to be short neurotoxins. Whole venom had an intravenous LD50 of 0.07 mg/kg in mice and showed a high phospholipase A2 activity, but no proteinase activity in vitro. Preclinical assessment of neutralization and ELISA immunoprofiling showed that BioCSL Sea Snake Antivenom was effective in cross-neutralizing A. laevis venom with an ED50 of 821 mu g venom per mL antivenom, with a binding preference towards short neurotoxins, due to the high degree of conservation between short neurotoxins from A. laevis and Enhydrina schistosa venom. Our results point towards the possibility of developing recombinant antibodies or synthetic inhibitors against A. laevis venom due to its simplicity. (C) 2015 Elsevier Ltd. All rights reserved.
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